Repository of University of Nova Gorica

Show document
A+ | A- | Help | SLO | ENG

Title:Entropic cost of folding and phase diagrams of polypeptides: Why are IDPs unfolded at room temperature?
Authors:ID Badasyan, Artem, Univerza v Novi Gorici (Author)
Files: This document has no files that are freely available to the public. This document may have a physical copy in the library of the organization, check the status via COBISS. Link is opened in a new window
Language:English
Work type:Not categorized
Typology:3.14 - Invited Lecture at Foreign University
Organization:UNG - University of Nova Gorica
Abstract:In spin models, that are applied to describe the conformational transitions in polymers, the number of spin orientations, that correspond to the disordered conformation, can be estimated using fundamental definitions of Statistical Physics. For instance, when considering alpha-helix to coil transition in polypeptides, the role of generalized coordinates is played by pairs of torsional angle, and the repeating unit populates different regions of that 2D contour map, depending on conformation. By scanning over all possible torsional angles, that do not violate the obvious limitations due to the excluded volume, the so-called Ramachandran map can be plotted, which is actually the phase space visualization for the helix-coil transition problem. The region of phase space, corresponding to the ordered, helical conformations, is much more limited, than the one, corresponding to all other (allowed) conformations. We can calculate the areas of these regions as Γhelix and Γcoil , and construct the ratio Q = Γcoil . Naturally, it can be interpreted as log(Q) = Scoil − Shelix = ΔS, the entropic cost of helix with respect to coil. To illustrate the importance of the entropic price of ordered conformation we report our recent results, that allowed to explain the peculiarity of phase diagrams of Intrinsically Disordered Proteins (IDP) out of larger Q-values, as compared to globular counterparts. In particular, it has been shown, that due to larger Q, the phase diagram of IDP is shifted towards higher temperatures.
Keywords:IDP, protein folding, phase diagram
Place of performance:Dept. of Physics, Free University of Berlin, Arnimallee 14 14195 Berlin, Germany
Year of performance:2016
PID:20.500.12556/RUNG-2460 New window
COBISS.SI-ID:4407291 New window
NUK URN:URN:SI:UNG:REP:NZVCQ2J3
Publication date in RUNG:23.06.2016
Views:4633
Downloads:0
Metadata:XML RDF-CHPDL DC-XML DC-RDF
:
Copy citation
  
Average score:(0 votes)
Your score:Voting is allowed only for logged in users.
Share:Bookmark and Share


Hover the mouse pointer over a document title to show the abstract or click on the title to get all document metadata.

Back